| pubmed-article:15239672 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15239672 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:15239672 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:15239672 | lifeskim:mentions | umls-concept:C0205374 | lld:lifeskim |
| pubmed-article:15239672 | lifeskim:mentions | umls-concept:C0245758 | lld:lifeskim |
| pubmed-article:15239672 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:15239672 | pubmed:dateCreated | 2004-9-1 | lld:pubmed |
| pubmed-article:15239672 | pubmed:abstractText | Magnesium protoporphyrin IX methyltransferase (ChlM), an enzyme in the chlorophyll biosynthetic pathway, catalyses the transfer of a methyl group to magnesium protoporphyrin IX (MgP) to form magnesium protoporphyrin IX monomethyl ester (MgPME). S-Adenosyl-L-methionine is the other substrate, from which a methyl group is transferred to the propionate group on ring C of the porphyrin macrocycle. Stopped-flow techniques were used to characterize the binding of porphyrin substrate to ChlM from Synechocystis PCC6803 by monitoring tryptophan fluorescence quenching on a millisecond timescale. We concluded that a rapid binding step is preceded by a slower isomerization of the enzyme. Quenched-flow techniques have been employed to characterize subsequent partial reactions in the catalytic mechanism. A lag phase has been identified that has been attributed to the formation of an intermediate. Our results provide a greater understanding of this catalytic process which controls the relative concentrations of MgP and MgPME, both of which are implicated in signalling between the plastid and nucleus in plants. | lld:pubmed |
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| pubmed-article:15239672 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15239672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15239672 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15239672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15239672 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15239672 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:15239672 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:15239672 | pubmed:author | pubmed-author:HunterC... | lld:pubmed |
| pubmed-article:15239672 | pubmed:author | pubmed-author:ShepherdMarkM | lld:pubmed |
| pubmed-article:15239672 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15239672 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:15239672 | pubmed:volume | 382 | lld:pubmed |
| pubmed-article:15239672 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15239672 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15239672 | pubmed:pagination | 1009-13 | lld:pubmed |
| pubmed-article:15239672 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:meshHeading | pubmed-meshheading:15239672... | lld:pubmed |
| pubmed-article:15239672 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15239672 | pubmed:articleTitle | Transient kinetics of the reaction catalysed by magnesium protoporphyrin IX methyltransferase. | lld:pubmed |
| pubmed-article:15239672 | pubmed:affiliation | Robert Hill Institute for Photosynthesis and Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK. shepherd@secsg.uga.edu | lld:pubmed |
| pubmed-article:15239672 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15239672 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15239672 | lld:pubmed |
